4:00pm
Tuesday, October 30, 2012
Brandeis University
Joint Quantitative Biology Program/Physics Department Colloquium
Abelson 131
Douglas Weibel
University of Wisconsin, Madison
Co-sponsored with the Quantitative Biology Program
Protein regulation at curved bacterial membranes
Refreshments at 3:30pm outside Abelson 131
Abstract: Using a combination of cell biological, biochemical, and biophysical techniques, we demonstrate that the Escherichia coli recombination repair enzyme, RecA is temporally localized and regulated by its interaction with anionic phospholipids at regions of large, negative membrane curvature. Early studies on RecA function in vivo demonstrated large amounts of protein associating with membrane fractions during DNA damage (Garvey et al. 1985, J. Biol. Chem. 285, 18984). A fundamental unanswered question is why does RecA bind the membrane and is this interaction conserved across organisms? To test whether this mechanism is evolutionarily conserved between bacteria and mitochondria, we are extending our studies to Rad51, which is a mitochondrial homolog of RecA. Recent studies have implicated Rad51 in mtDNA repair during damage due to lipid peroxidation. In this presentation I discuss several possible hypotheses that support our data.